Curated BLAST for Genomes

 

Curated BLAST

Searching in Pedobacter sp. GW460-11-11-14-LB5 (Pedo557)

Found 65 curated entries in PaperBLAST's database that match '3.7.1.2'.

These curated entries have 46 distinct sequences.

Running ublast with E ≤ 0.01

Found 7 relevant proteins in Pedobacter sp. GW460-11-11-14-LB5, or try another query

CA265_RS08350: ureidoglycolate lyase
is similar to:
PaperBLAST

C785_RS20550 / A0A2E7P912: 5-hydroxy-2,4-dioxopentanoate hydrolase (EC 3.7.1.26) from Herbaspirillum sp.

55% id,
98% cov

HSERO_RS06355: 2,4-diketo-3-deoxy-L-fuconate hydrolase (EC 3.7.1.26) from Herbaspirillum seropedicae

55% id,
98% cov

BMULJ_04921 / A0A0H3KT28: 2,4-didehydro-3-deoxy-L-fuconate hydrolase (EC 3.7.1.26) from Burkholderia multivorans

53% id,
100% cov

More...

CA265_RS15165: 2-hydroxyhepta-2,4-diene-1,7-dioate isomerase
is similar to:
PaperBLAST

A0A0D5YDA5: fumarylacetoacetase (EC 3.7.1.2) from Acinetobacter baumannii

39% id,
91% cov

A0A0M3SVN7: fumarylacetoacetase (EC 3.7.1.2) from Cupriavidus gilardii

37% id,
87% cov

naaD / F8QQ75: 3-fumarylpyruvate hydrolase (EC 3.7.1.20) from Bradyrhizobium sp.

38% id,
82% cov

More...

CA265_RS03145: fumarylacetoacetate hydrolase
is similar to:
PaperBLAST

BMULJ_04921 / A0A0H3KT28: 2,4-didehydro-3-deoxy-L-fuconate hydrolase (EC 3.7.1.26) from Burkholderia multivorans

28% id,
97% cov

HBZF_PSEAC / Q0QFQ3: Maleylpyruvate hydrolase; MPH11; EC 3.7.1.23 from Pseudomonas alcaligenes
hbzF / Q0QFQ3: maleylpyruvate hydrolase monomer (EC 3.7.1.23) from Pseudomonas alcaligenes
Q0QFQ3: maleylpyruvate hydrolase (EC 3.7.1.23) from Pseudomonas alcaligenes

27% id,
99% cov

K0A9N9: fumarylacetoacetase (EC 3.7.1.2) from Exiguobacterium antarcticum

27% id,
99% cov

More...

CA265_RS15805: acetolactate synthase, large subunit, biosynthetic type
is similar to:
PaperBLAST

IOLD_BACSU / P42415: 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase; THcHDO hydrolase; EC 3.7.1.22 from Bacillus subtilis
iolD / P42415: 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase (EC 3.7.1.22) from Bacillus subtilis
P42415: 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione acylhydrolase (ring-opening) (EC 3.7.1.22) from Bacillus subtilis

26% id,
93% cov

AO356_23185: 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase IolD (EC 3.7.1.22) from Pseudomonas fluorescens

27% id,
88% cov

PS417_11870: 3D-(3,5/4)-trihydroxycyclohexane-1,2-dione hydrolase IolD (EC 3.7.1.22) from Pseudomonas simiae

27% id,
88% cov

More...

CA265_RS15100: alpha/beta hydrolase
is similar to:
PaperBLAST

TODF_PSEP1 / P23133: 2-hydroxy-6-oxo-2,4-heptadienoate hydrolase; HOHH; EC 3.7.1.25 from Pseudomonas putida
todF / P23133: 2-hydroxy-6-oxohepta-2,4-dienoate hydrolase (EC 3.7.1.25) from Pseudomonas putida

25% id,
91% cov

CA265_RS20005: enoyl-CoA hydratase
is similar to:
PaperBLAST

BAMA_GEOMG / Q39TV7: 6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase; 6-OCH-CoA hydrolase; 6-oxocyclohex-1-ene-1-carbonyl-CoA hydratase; EC 3.7.1.21 from Geobacter metallireducens

30% id,
50% cov

BAMA_THAAR / O87872: 6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase; 6-oxocyclohex-1-ene-1-carbonyl-CoA hydratase; Beta-oxoacyl-CoA hydrolase; Oah; EC 3.7.1.21 from Thauera aromatica
O87872: 6-oxocyclohex-1-ene-1-carbonyl-CoA hydratase (EC 3.7.1.21) from Thauera aromatica

28% id,
51% cov

BAMA_SYNAS / Q2LXU2: 6-oxocyclohex-1-ene-1-carbonyl-CoA hydrolase; 6-OCH-CoA hydrolase; 6-oxocyclohex-1-ene-1-carbonyl-CoA hydratase; EC 3.7.1.21 from Syntrophus aciditrophicus
bamA / Q2LXU2: 6-oxocyclohex-1-ene-1-carbonyl-CoA hydratase monomer (EC 3.7.1.21) from Syntrophus aciditrophicus

30% id,
37% cov

CA265_RS13890: alpha/beta hydrolase
is similar to:
PaperBLAST

TODF_PSEP1 / P23133: 2-hydroxy-6-oxo-2,4-heptadienoate hydrolase; HOHH; EC 3.7.1.25 from Pseudomonas putida
todF / P23133: 2-hydroxy-6-oxohepta-2,4-dienoate hydrolase (EC 3.7.1.25) from Pseudomonas putida

28% id,
47% cov

The hits are sorted by %identity * %coverage (highest first)

Running ublast against the 6-frame translation. All reading frames of at least 30 codons are included.

Found hits to 7 reading frames. These were all redundant with annotated proteins.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory